Muhammet Güler, Zehra Başı, Vedat Türkoğlu, M. Rıza Kıvanç

Van Gölü Balığı Beyin ve Karaciğerindeki Asetilkolinesteraz (EC 3.1.1.7) Enzimi Üzerine Bazı Bitki Özütlerinin İn vitro Etkileri

Bu çalışmada; sinir uyarılarının naklinden görevli enzim olan Van Gölü balığı (Chalcalburnus tarichi P.1811) karaciğer ve beyin asetilkolinesteraz (EC 3.1.1.7) enzimi üzerine meyan [Glycyrrhiza glabra L. (Leguminosae)], anason [Pimpinella anisum L. (Umbelliferae)] ve papatya [Matricaria chamomilla L. (Compositae)] özütlerinin etkisi araştırılmıştır. Bu özütler balık karaciğer AChE’ni active ederken balık beyin AChE’ni inhibe etmiştir. Kullanılan bitkiler balık beyni AChE üzerine yarışmasız inhibisyon göstermiştir. $I{_50}$ değerleri meyan için 1,714 $mg.mL^{-1}$, anason için 0,394 $mg.mL^{-1}$ ve papatya için 0,604 mg.ml-1 olarak bulunmuştur. Karaciğer ve beyin AcHE için optimum sıcaklık 30oC ve optimum pH sırasıyla 6-8 ve 6-8,5 olarak bulunmuştur. Ek olarak balık beyin ve karaciğer AChE’nin spesifik aktiviteleri sırasıyla 130,5 EU.mg-1 ve 13,59 EU.mg-1 olarak bulunmuştur.

In vitro Effects of Certain Plant Extracts on Acetylcholinesterase (EC 3.1.1.7) Enzyme in Lake Van Fish Liver and Brain

In this study, the effect of Glycyrrhiza glabra (Leguminosae), Pimpinella anisum (Umbelliferae) and Matricaria chamomilla (Compositae) extracts on both Lake Van fish (Chalcalburnus tarichi P.1811) brain and liver acetylcholinesterase enzymes (AChE) activity, responsible for transformation of nerve stimulations, has been investigated. While activating fish liver AChE, these extracts inhibited fish brain AChE activity. The plants used in the showed noncompetitive inhibition on the fish brain AChE. $I{_50}$ values were estimated 1.714 mg.mL-1 for Glycyrrhiza glabra, 0.604 $mg.mL^{-1}$ for Matricaria chamomilla and 0.394 $mg.mL^{-1}$ for Pimpinella anisum. The optimum temperature for liver and brain AChE was found to be 30°C and optimum pH of 6-8.5 and 6-8 respectively. In addition, specific activities of fish brain and liver AChE were found 130.5 EU.mg-1 and 13.59 EU.mg-1 respectively.

PDF

___

1. M. Citron, Beta-secretase inhibition for the treatment of Alzheimer’s disease-promise and chellenge, Trends in Pharmacological Sciences, 25 (2004) 92–97.
2. D.K. Lahiri, M.R. Farlow, N.H. Greig, K. Sambamurti, Current drug targets for Alzheimer’s disease treatment, Drug Development Research, 56 ( 2002) 267–281.
3. M. Heinrich, H.L. Teoh, Galanthamine from snowdropthe development of a modern drug against Alzheimer’s disease from local Caucasian knowledge, Journal of Ethnopharmacology, 92 (2004) 147–162.
4. O. Maschi, E. Dal Cero, G.V. Gali, D. Caruso, E. Bosisio, M. Dell’Agli, Inhibition of human cAMPPhosphodiesterase as a mechanism of the spasmolytic effect of Matricaria recutita L., Journal of Agricultural and Food Chemistry, 56 (2008) 5015– 5020.
5. M.A. Boelens, Spices and condiments II In Volatile Compounds in Food and Beverages, H. Maarse (Ed.), pp. Marcel Dekker, Inc., New York, Basel, Hong Kong, (1991) 449–482.
6. N.G. Bisset (Ed.), Herbal Drugs and Phytopharmaceuticals. CRC Press, Medpharm, Stuttgart, (1994) pp. 73–75.
7. Z. Aboabrahim, Z. Kharazmshahi, vol. 2. National Works Publications, Teheran, (1970) p. 141.
8. Y. Asada, W.Li, T. Yoshikawa, Biosynthesis of the dimethylallyl moiety of glabrol in Glycyrrhiza glabra hairy root cultures via a non-mevalonate pathway, Phytochemistry, 55 (2000) 323–326.
9. T. Baytop, Treatment with Plants in Turkey, Past and Present, , İstanbul, 1999.
10. A.Yalçın, Encyclopedia of Medicinal Plants Home drugs/ healing Waters. Gateway Publications, 1996.
11. E.A. Demirhan, The Place of Liauorice in the History of Medicine, Its Importance from the point of Wiew of Traditinol Treatments and Some Samples from İstanbul and Bursa Herbalists, Turkey Clinics J. Med Ethics., 12 (2004) 248-252.
12. A. Ozdemir, V. Turkoglu, H. Demir, In vitro effect of some plant extracts on acetylcholinesterase enzyme in human erythrocytes and serum, Fresenius Environmental Bulletin, 22 (2013) 2510-2515.
13. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72 (1976) 48-51.
14. G.L. Ellman, K.O. Courtney, V. Andres, Feather-Stone RM A new and rapid colorimetric determination of acetylcholinesterase activity, Biochem. Pharmacol., 7 (1961) 88-95.
15. H. Lineweaver, D. Burk, The determination of enzyme dissociation constants, J Am Chem Soc., 56 (1934) 658–660.
16. P. Scaps, O. Borot, Acetylcholinesterase Activity of the Polyhaete Nereis Diversicolor: of Effects Temperature, Salinity, Comp. Biochem. Physiol., 125 (2000) 377-383.
17. Ö.F. Güloğlu, V. Türkoğlu, İ. Çelik, Purification and Characterization of Acetylcholinesterase from Sheep Liver and Inhibition by some Poinkillers, Asian Journal of Chemistry, 13 ( 2006) 1097-1103.
18. E. Akman, V. Türkoğlu, İ. Çelik, Purification and characterization of Van lake fish (Chalcalburnus tarichii P.1811) liver and brain acetylcholinesterase, Hacettepe Journal of Biology and Chemistry, 37 (2009) 331-336.